Structure of mammalian steroid receptors: evolving concepts and methodological developments.

Structure of mammalian steroid receptors: evolving concepts and methodological developments.
复制标题

哺乳动物类固醇受体的结构:概念的演变和方法的发展。

DOI:
10.1146/annurev.ph.46.030184.000503
复制
发表时间:
1984
影响因子:
18.2
通讯作者:
Stevens,J
Stevens,J
中科院分区:
医学1区
文献类型:
--
作者:
Sherman,MR;Stevens,J

文献摘要

被引文献

相似文献

尽管在从哺乳动物组织中提取的类固醇受体的稳定化、纯化和结构分析方面做了大量工作并取得了重大进展,但天然状态仍然在很大程度上未知。已检测到来自同一组织的单一类别类固醇的受体以各种分子形式和至少三种功能状态存在。在这篇综述中,这些状态被称为未转化状态、转化状态和不活跃状态。它们的区别在于受体对类固醇的亲和力和类固醇-受体复合物对细胞核、DNA和离子树脂的亲和力的差异。未转化的类固醇-受体复合物可在低温下与类固醇孵育的细胞或组织的细胞质提取物(细胞质溶胶)中检测到,或在低温和低离子强度下与类固醇孵育的细胞质溶胶中检测到。这些复合物的特征在于对细胞核、染色质、DNA或阴离子树脂(如DNA-纤维素或ATP-琼脂糖)的低亲和力,以及对阳离子树脂(如DEAE-纤维素或DEAE-琼脂糖)的高亲和力[综述见(15,31,63,92)]。转化,定义为获得对细胞核、DNA和阴离子树脂的高亲和力,通过将在冷条件下与类固醇一起孵育的细胞加温(68,69,123 a)或通过对含类固醇的细胞质溶胶的各种操作,如延长储存、稀释、凝胶化等来实现。
Despite much work and significant progress on the stabilization, purification, and structural analysis of steroid receptors extracted from mammalian tissues, the native state still remains largely unknown. Receptors for a single class of steroids from the same tissue have been detected in various molecular forms and at least three functional states. In this review, these states are referred to as the untransformed, transformed, and inactive states. They are distinguished by differences in the affinity of the receptor for steroids and in the affinity of the steroid-receptor complex for nuclei, DNA, and ionic resins. The untransformed steroid-receptor complexes are detected in cytoplasmic extracts (cytosols) of cells or tissues that were incubated with steroid in the cold, or in cytosols incubated with steroid at low temperature and low ionic strength. These complexes are characterized by low affinity for nuclei, chromatin, DNA, or anionic resins, such as DNA-cellulose or ATP-agarose, and high affinity for cationic resins, such as DEAE-cellulose or DEAE-agarose [reviewed in (15, 31, 63, 92)]. Transformation, defined as the acquisition of high affinity for nuclei, DNA, and anionic resins, is effected by warming cells that were incubated in the cold with steroid (68, 69, 123a) or by various manipulations of steroid-containing cytosols, such as prolonged storage, dilution, gel